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Updated: Jul 16, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
AFM structural study of the molecular chaperone GroEL and its two-dimensional crystals: an ideal "living" calibration
F Valle1, J A DeRose, G Dietler
1Institut de Physique de la Matière Condensèe, BSP, Université de Lausanne, Dorigny, Switzerland. francesco.valle@ipmc.unil.ch
Abstract:
Supramolecular complexes, such as chaperonins, are suitable samples for atomic force microscope structural studies because they have a very well defined shape. High-resolution images can be made using tapping mode in liquid under native conditions. Details about the two-dimensional structures formed onto the surface upon adsorption and of the single protein can be observed. Dissection of the upper ring of the supramolecular complex as a result of the applied lateral force through scanning tip is observed. Finally, the combination of lateral convolution and tip penetration into the cavity of chaperonins offers a direct evaluation of the tip convolution effect on images of macromolecular samples.
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